ID A0A3N5AYJ2_9BACI Unreviewed; 758 AA.
AC A0A3N5AYJ2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN ORFNames=EDC24_2864 {ECO:0000313|EMBL:RPF50049.1};
OS Aquisalibacillus elongatus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Aquisalibacillus.
OX NCBI_TaxID=485577 {ECO:0000313|EMBL:RPF50049.1, ECO:0000313|Proteomes:UP000276443};
RN [1] {ECO:0000313|EMBL:RPF50049.1, ECO:0000313|Proteomes:UP000276443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18090 {ECO:0000313|EMBL:RPF50049.1,
RC ECO:0000313|Proteomes:UP000276443};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU003410};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, ECO:0000256|RuleBase:RU003410}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RPF50049.1}.
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DR EMBL; RKRF01000014; RPF50049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5AYJ2; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000276443; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000276443}.
FT DOMAIN 616..638
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 758 AA; 87098 MW; CB19A153BF87D52B CRC64;
MTVKTEPIIV TEGGVYQERF DEQQLRDYLL GLLIDFEELD GATFTEKIIQ SVITKESITK
EQITNEVLLR GLENISPEEP NWTYVCSRVY LDQLYKKASL NRGYSRMQKY GNLYELTRYL
TKINIFSDQL LTYYDQNEFE ELASIIEPER DQLFTYIGIR TLADRYLAKD HEGRIYELPQ
ERFLIIAMSL MIYEPKEKRL DLVKEAYWAM SNLYMTVATP TLSNAGKAHG QLSSCFIDTV
DDSLQGIYDS NTDIANLSKN GGGIGVYLGK IRSHGSSIKG FKGISSGVMP WMKQLNNTAV
SVDQLGQRQG AIAVYLDVWH KDIHKFLDAK LNNGDERQRT HDLFTGVTLP DLFMEKVEAR
ENWYLFDPHE VREVMGYSLE DYYDEEDGKG SFREKYEECV NHQGLSKEEV PAIDLMKRIM
ISQLETGTPF MFYRDEVNRK NPNRHKGMIY SSNLCTEITQ NQSPTTVEEQ FTEDGKIIVT
KNPGDFVVCN LSSINLGKAV TSGVLERLIP IQVRMLDNVI DLNDIPVLQA QIANQKYRAV
GLGTFGYHHL LALIGFRWES EEAVEFADHL YEQIAYLTIK ASNDLAKEKG AYPSFEGSDW
SNGQYFEKRG YHSPEWNKLK EKVQKHGVRN GYLMAVAPNS STSLIAGSTA SIDPIFKKFY
SEEKKDYKIP VTAPDLSPKT FWLYKSAYDI DHQWTIKQNE ARQKHIDQSI SFNFYVRNNI
KAKELLDLHL SAWKSKFKTT YYTRSTSSEI EDCVSCES
//